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Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
The apposed membranes of myelinating Schwann cells are joined by several types of junctional specializations known as autotypic or reflexive junctions. These include tight, gap, and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2002
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173042/ https://www.ncbi.nlm.nih.gov/pubmed/12403818 http://dx.doi.org/10.1083/jcb.200207050 |
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author | Poliak, Sebastian Matlis, Sean Ullmer, Christoph Scherer, Steven S. Peles, Elior |
author_facet | Poliak, Sebastian Matlis, Sean Ullmer, Christoph Scherer, Steven S. Peles, Elior |
author_sort | Poliak, Sebastian |
collection | PubMed |
description | The apposed membranes of myelinating Schwann cells are joined by several types of junctional specializations known as autotypic or reflexive junctions. These include tight, gap, and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman, and mesaxons. The molecular components of autotypic tight junctions have not been established. Here we report that two homologues of Discs Lost–multi PDZ domain protein (MUPP)1, and Pals-associated tight junction protein (PATJ), are differentially localized in myelinating Schwann cells and associated with different claudins. PATJ is mainly found at the paranodal loops, where it colocalized with claudin-1. MUPP1 and claudin-5 colocalized in the incisures, and the COOH-terminal region of claudin-5 interacts with MUPP1 in a PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner. In developing nerves, claudin-5 and MUPP1 appear together in incisures during the first postnatal week, suggesting that they coassemble during myelination. Finally, we show that the incisures also contain four other PDZ proteins that are found in epithelial tight junctions, including three membrane-associated guanylate-kinase proteins (membrane-associated guanylate-kinase inverted-2, ZO-1, and ZO-2) and the adaptor protein Par-3. The presence of these different tight junction proteins in regions of noncompact myelin may be required to maintain the intricate cytoarchitecture of myelinating Schwann cells. |
format | Text |
id | pubmed-2173042 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2002 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21730422008-05-01 Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells Poliak, Sebastian Matlis, Sean Ullmer, Christoph Scherer, Steven S. Peles, Elior J Cell Biol Article The apposed membranes of myelinating Schwann cells are joined by several types of junctional specializations known as autotypic or reflexive junctions. These include tight, gap, and adherens junctions, all of which are found in regions of noncompact myelin: the paranodal loops, incisures of Schmidt-Lanterman, and mesaxons. The molecular components of autotypic tight junctions have not been established. Here we report that two homologues of Discs Lost–multi PDZ domain protein (MUPP)1, and Pals-associated tight junction protein (PATJ), are differentially localized in myelinating Schwann cells and associated with different claudins. PATJ is mainly found at the paranodal loops, where it colocalized with claudin-1. MUPP1 and claudin-5 colocalized in the incisures, and the COOH-terminal region of claudin-5 interacts with MUPP1 in a PSD-95/Disc Large/zona occludens (ZO)-1 (PDZ)-dependent manner. In developing nerves, claudin-5 and MUPP1 appear together in incisures during the first postnatal week, suggesting that they coassemble during myelination. Finally, we show that the incisures also contain four other PDZ proteins that are found in epithelial tight junctions, including three membrane-associated guanylate-kinase proteins (membrane-associated guanylate-kinase inverted-2, ZO-1, and ZO-2) and the adaptor protein Par-3. The presence of these different tight junction proteins in regions of noncompact myelin may be required to maintain the intricate cytoarchitecture of myelinating Schwann cells. The Rockefeller University Press 2002-10-28 /pmc/articles/PMC2173042/ /pubmed/12403818 http://dx.doi.org/10.1083/jcb.200207050 Text en Copyright © 2002, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Poliak, Sebastian Matlis, Sean Ullmer, Christoph Scherer, Steven S. Peles, Elior Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title | Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title_full | Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title_fullStr | Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title_full_unstemmed | Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title_short | Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells |
title_sort | distinct claudins and associated pdz proteins form different autotypic tight junctions in myelinating schwann cells |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173042/ https://www.ncbi.nlm.nih.gov/pubmed/12403818 http://dx.doi.org/10.1083/jcb.200207050 |
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